A lipid-anchored binding protein is a component of an ATP-dependent cellobiose/cellotriose-transport system from the cellulose degrader Streptomyces reticuli

Eur J Biochem. 1996 Dec 1;242(2):332-8. doi: 10.1111/j.1432-1033.1996.0332r.x.


During cultivation in the presence of cellobiose or crystalline cellulose, Streptomyces reticuli expresses an inducible uptake system that transports cellobiose (K(m), 4 microM), cellotriose and, to a lesser degree, cellotetraose and cellopentaose. Cellobiose uptake is dependent on ATP and inhibited by N-ethylmaleimide. A binding protein was identified in its palmitylated form in the cytoplasmic membrane of mycelia. It could be extracted with the detergent Triton X-100 and purified by two subsequent anion-exchange chromatographies. It showed highest affinity (Kd, 1.5 microM) for cellobiose and cellotriose. The data suggest that cellobiose/cellotriose uptake is mediated by a membrane-anchored lipoprotein as a component of an ATP-binding-cassette-transporter system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Biological Transport
  • Blotting, Western
  • Cell Membrane / metabolism
  • Cellobiose / metabolism*
  • Cellulose / metabolism
  • Circular Dichroism
  • Kinetics
  • Lipoproteins / chemistry*
  • Lipoproteins / isolation & purification
  • Lipoproteins / metabolism*
  • Protein Conformation
  • Spectrometry, Fluorescence
  • Streptomyces / metabolism*
  • Substrate Specificity
  • Trisaccharides / metabolism*
  • Tryptophan


  • Lipoproteins
  • Trisaccharides
  • Cellobiose
  • mannotriose
  • Tryptophan
  • Adenosine Triphosphate
  • Cellulose